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1-7 of 7
Keywords: amyloid
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Articles
Journal:
Bioscience Reports
Biosci Rep (2024) 44 (11): BSR20241102.
Published: 06 November 2024
... [ 20 ] AD, PD, CJD, Prion-associated diseases Insulin amyloid 80 µM In vitro 4, 10, and 24 h ↑ Amyloid degradation Girigoswami et al. , 2019 [ 33 ] AD, PD, Prion-associated diseases HEWL amyloid 10 µM In vitro 120 h ↓ Amyloid fibrillation Ban et al. , 2016 [ 34 ] PD 6-OHDA (50...
Articles
Journal:
Bioscience Reports
Biosci Rep (2023) 43 (10): BSR20230489.
Published: 03 October 2023
...Shalini Singh; Vibhuti Joshi; Arun Upadhyay Amyloids are high-order proteinaceous formations deposited in both intra- and extracellular spaces. These aggregates have tendencies to deregulate cellular physiology in multiple ways; for example, altered metabolism, mitochondrial dysfunctions, immune...
Articles
Journal:
Bioscience Reports
Biosci Rep (2022) 42 (5): BSR20211297.
Published: 18 May 2022
... (PMDs) and involves human islet amyloid polypeptide (hIAPP) misfolding and accumulating in parts of the body, primarily in the pancreas, causing damage to islet cells and affecting glucose regulation. In this review, we have summarised our current understanding of what causes hIAPP to misfold, what...
Includes: Supplementary data
Articles
Journal:
Bioscience Reports
Biosci Rep (2019) 39 (3): BSR20190327.
Published: 06 March 2019
... concentration. Cofactors such as glycosaminoglycans and metal ions have been found associated with amyloid deposits in vivo and shown to affect protein assembly kinetics in vitro. Cofactor interactions with the amyloidogenic process are an area of great interest for therapeutic intervention for the wide range...
Articles
Jie Sheng, Nick K. Olrichs, Willie J. Geerts, Xueyi Li, Ashfaq Ur Rehman, Barend M. Gadella, Dora V. Kaloyanova, J. Bernd Helms
Journal:
Bioscience Reports
Biosci Rep (2019) 39 (2): BSR20182345.
Published: 12 February 2019
... that is defined by four sequence motifs and a highly conserved tertiary structure. A common structure–function relationship for this domain is hitherto unknown. A characteristic of several CAP proteins is their formation of amyloid-like structures in the presence of lipids. Here we investigate the structural...
Includes: Supplementary data
Articles
Alexandr G. Bobylev, Oxana V. Galzitskaya, Roman S. Fadeev, Liya G. Bobyleva, Darya A. Yurshenas, Nikolay V. Molochkov, Nikita V. Dovidchenko, Olga M. Selivanova, Nikita V. Penkov, Zoya A. Podlubnaya, Ivan M. Vikhlyantsev
Journal:
Bioscience Reports
Biosci Rep (2016) 36 (3): e00334.
Published: 20 May 2016
...Alexandr G. Bobylev; Oxana V. Galzitskaya; Roman S. Fadeev; Liya G. Bobyleva; Darya A. Yurshenas; Nikolay V. Molochkov; Nikita V. Dovidchenko; Olga M. Selivanova; Nikita V. Penkov; Zoya A. Podlubnaya; Ivan M. Vikhlyantsev Amyloids are insoluble fibrous protein aggregates, and their accumulation...
Articles
Jerson L. Silva, Luciana P. Rangel, Danielly C. F. Costa, Yraima Cordeiro, Claudia V. De Moura Gallo
Journal:
Bioscience Reports
Biosci Rep (2013) 33 (4): e00054.
Published: 25 July 2013
..., the CTD (C-terminal domain) and the core domain (p53C) that constitutes the sequence-specific DBD (DNA-binding region). Most p53 mutations related to cancer development are found in the DBD. Aggregation of p53 into amyloid oligomers and fibrils has been shown. Moreover, amyloid aggregates of both...